The scope, efficiency, and practicality of synthesizing chiral organic catalysts that simulate some of the aspects of enzyme systems will be explored. Particular attention will be given to synthetic transacylases, transalkylases, hydrolases, and reductases. In the transacylases, the substrates will be amino esters and amino amides. The complexation between an alkylammonium ion and a macrocyclic polyether, which contains a nucleophile-leaving group and a chiral barrier, will collect and orient the substrate and the catalyst. In transalkylases, racemic carbon acid salts will be complexed and given "sidedness" by a chiral macrocyclic polyether and, hopefully, will be alkylated only from one side. In hydrolases, water will be added stereospecifically to fumarate complexed in a chiral environment. In reductases double bonds will be reduced stereospecifically by Rh bound to chiral ligands. Particular attention will be given to asymmetric selection in the desired catalyzed organic reactions. New rigid binding systems with convergent functional groups are being synthesized and tested.